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1dmy

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(New page: 200px<br /><applet load="1dmy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dmy, resolution 2.45&Aring;" /> '''COMPLEX BETWEEN MURI...)
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[[Image:1dmy.jpg|left|200px]]<br /><applet load="1dmy" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dmy, resolution 2.45&Aring;" />
 
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'''COMPLEX BETWEEN MURINE MITOCHONDRIAL CARBONIC ANYHDRASE V AND THE TRANSITION STATE ANALOGUE ACETAZOLAMIDE'''<br />
 
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==Overview==
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==COMPLEX BETWEEN MURINE MITOCHONDRIAL CARBONIC ANYHDRASE V AND THE TRANSITION STATE ANALOGUE ACETAZOLAMIDE==
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The three-dimensional structure of murine mitochondrial carbonic anhydrase, V has been determined and refined at 2.45-A resolution (crystallographic R, factor = 0.187). Significant structural differences unique to the active, site of carbonic anhydrase V are responsible for differences in the, mechanism of catalytic proton transfer as compared with other carbonic, anhydrase isozymes. In the prototypical isozyme, carbonic anhydrase II, catalytic proton transfer occurs via the shuttle group His-64; carbonic, anhydrase V has Tyr-64, which is not an efficient proton shuttle due in, part to the bulky adjacent side chain of Phe-65. Based on analysis of the, structure of carbonic anhydrase V, we speculate that Tyr-131 may, participate in proton transfer due to its proximity to zinc-bound solvent, its solvent accessibility, and its electrostatic environment in the, protein structure. Finally, the design of isozyme-specific inhibitors is, discussed in view of the complex between carbonic anhydrase V and, acetazolamide, a transition-state analogue. Such inhibitors may be, physiologically important in the regulation of blood glucose levels.
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<StructureSection load='1dmy' size='340' side='right'caption='[[1dmy]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dmy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DMY FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AZM:5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE'>AZM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dmy OCA], [https://pdbe.org/1dmy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dmy RCSB], [https://www.ebi.ac.uk/pdbsum/1dmy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dmy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CAH5A_MOUSE CAH5A_MOUSE] Reversible hydration of carbon dioxide. Low activity.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dm/1dmy_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dmy ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1DMY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with ZN and AZM as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DMY OCA].
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*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structure determination of murine mitochondrial carbonic anhydrase V at 2.45-A resolution: implications for catalytic proton transfer and inhibitor design., Boriack-Sjodin PA, Heck RW, Laipis PJ, Silverman DN, Christianson DW, Proc Natl Acad Sci U S A. 1995 Nov 21;92(24):10949-53. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7479916 7479916]
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[[Category: Large Structures]]
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[[Category: Carbonate dehydratase]]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Boriack-Sjodin PA]]
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[[Category: Boriack-Sjodin, P.A.]]
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[[Category: Christianson DW]]
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[[Category: Christianson, D.W.]]
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[[Category: AZM]]
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[[Category: ZN]]
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[[Category: proton transfer]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:25:23 2007''
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Current revision

COMPLEX BETWEEN MURINE MITOCHONDRIAL CARBONIC ANYHDRASE V AND THE TRANSITION STATE ANALOGUE ACETAZOLAMIDE

PDB ID 1dmy

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